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Article: Cumulus-associated α2-macroglobulin derivative retains proconceptive glycodelin-C in the human cumulus matrix
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TitleCumulus-associated α2-macroglobulin derivative retains proconceptive glycodelin-C in the human cumulus matrix
 
AuthorsChung, MK2
Chiu, PCN2
Lee, CL2
Pang, RTK2
Ng, EHY2
Lee, KF2
Koistinen, R1
Koistinen, H1
Seppala, M1
Yeung, WSB2
 
KeywordsΑ2-Macroglobulin
Cumulus Matrix
Glycodelin
Hyaluronic Acid
Spermatozoa
 
Issue Date2009
 
PublisherOxford University Press. The Journal's web site is located at http://humrep.oxfordjournals.org/
 
CitationHuman Reproduction, 2009, v. 24 n. 11, p. 2856-2867 [How to Cite?]
DOI: http://dx.doi.org/10.1093/humrep/dep265
 
AbstractBACKGROUNDGlycodelin-C is a glycodelin isoform isolated from the cumulus matrix. It stimulates spermatozoa-zona pellucida binding. Here, we report the isolation and characterization of a novel glycodelin interacting protein (GIP) from human cumulus matrix.METHODSGIP was purified by liquid chromatograph and identified by mass spectrometry. The interaction of GIP with glycodelin, matrix molecule and spermatozoa were investigated. RESULTS Mass spectrometry analysis suggested that GIP contained the N-terminal region of α2-macroglobulin, confirmed by western blot with anti-α2-macroglobulin antibody. GIP bound to native but not deglycosylated glycodelin-C in native gel electrophoresis, suggesting that the binding was glycosylation-dependent. GIP did not bind to capacitated and uncapacitated human spermatozoa. The cumulus cells could convert exogenous labeled α2-macroglobulin into GIP in vitro. GIP interacted with hyaluronic acid, a major component of the cumulus matrix. Glycodelin-C bound to hyaluronic acid-coated agarose beads in the presence of GIP. Human spermatozoa acquired the hyaluronic acid-GIP-bound glycodelin-C during incubation in vitro. CONCLUSION The hyaluronic acid-GIP complex formed in the cumulus matrix retains and concentrates glycodelin-C in the cumulus matrix for displacing sperm-bound glycodelin-A and-F and stimulating the zona binding activity of the spermatozoa traversing through the cumulus mass.
 
ISSN0268-1161
2013 Impact Factor: 4.585
 
DOIhttp://dx.doi.org/10.1093/humrep/dep265
 
ISI Accession Number IDWOS:000271107700025
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorChung, MK
 
dc.contributor.authorChiu, PCN
 
dc.contributor.authorLee, CL
 
dc.contributor.authorPang, RTK
 
dc.contributor.authorNg, EHY
 
dc.contributor.authorLee, KF
 
dc.contributor.authorKoistinen, R
 
dc.contributor.authorKoistinen, H
 
dc.contributor.authorSeppala, M
 
dc.contributor.authorYeung, WSB
 
dc.date.accessioned2012-10-30T06:29:33Z
 
dc.date.available2012-10-30T06:29:33Z
 
dc.date.issued2009
 
dc.description.abstractBACKGROUNDGlycodelin-C is a glycodelin isoform isolated from the cumulus matrix. It stimulates spermatozoa-zona pellucida binding. Here, we report the isolation and characterization of a novel glycodelin interacting protein (GIP) from human cumulus matrix.METHODSGIP was purified by liquid chromatograph and identified by mass spectrometry. The interaction of GIP with glycodelin, matrix molecule and spermatozoa were investigated. RESULTS Mass spectrometry analysis suggested that GIP contained the N-terminal region of α2-macroglobulin, confirmed by western blot with anti-α2-macroglobulin antibody. GIP bound to native but not deglycosylated glycodelin-C in native gel electrophoresis, suggesting that the binding was glycosylation-dependent. GIP did not bind to capacitated and uncapacitated human spermatozoa. The cumulus cells could convert exogenous labeled α2-macroglobulin into GIP in vitro. GIP interacted with hyaluronic acid, a major component of the cumulus matrix. Glycodelin-C bound to hyaluronic acid-coated agarose beads in the presence of GIP. Human spermatozoa acquired the hyaluronic acid-GIP-bound glycodelin-C during incubation in vitro. CONCLUSION The hyaluronic acid-GIP complex formed in the cumulus matrix retains and concentrates glycodelin-C in the cumulus matrix for displacing sperm-bound glycodelin-A and-F and stimulating the zona binding activity of the spermatozoa traversing through the cumulus mass.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationHuman Reproduction, 2009, v. 24 n. 11, p. 2856-2867 [How to Cite?]
DOI: http://dx.doi.org/10.1093/humrep/dep265
 
dc.identifier.citeulike5426223
 
dc.identifier.doihttp://dx.doi.org/10.1093/humrep/dep265
 
dc.identifier.epage2867
 
dc.identifier.isiWOS:000271107700025
 
dc.identifier.issn0268-1161
2013 Impact Factor: 4.585
 
dc.identifier.issue11
 
dc.identifier.pmid19625311
 
dc.identifier.scopuseid_2-s2.0-70350510673
 
dc.identifier.spage2856
 
dc.identifier.urihttp://hdl.handle.net/10722/173353
 
dc.identifier.volume24
 
dc.languageeng
 
dc.publisherOxford University Press. The Journal's web site is located at http://humrep.oxfordjournals.org/
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofHuman Reproduction
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshChromatography, Liquid
 
dc.subject.meshCumulus Cells - metabolism
 
dc.subject.meshExtracellular Matrix Proteins - metabolism
 
dc.subject.meshFemale
 
dc.subject.meshGlycoproteins - metabolism
 
dc.subject.meshGlycosylation
 
dc.subject.meshHumans
 
dc.subject.meshHyaluronic Acid - metabolism
 
dc.subject.meshMale
 
dc.subject.meshMass Spectrometry
 
dc.subject.meshPregnancy Proteins - metabolism
 
dc.subject.meshProtein Isoforms - metabolism
 
dc.subject.meshSpermatozoa - metabolism
 
dc.subject.meshalpha-Macroglobulins - metabolism
 
dc.subjectΑ2-Macroglobulin
 
dc.subjectCumulus Matrix
 
dc.subjectGlycodelin
 
dc.subjectHyaluronic Acid
 
dc.subjectSpermatozoa
 
dc.titleCumulus-associated α2-macroglobulin derivative retains proconceptive glycodelin-C in the human cumulus matrix
 
dc.typeArticle
 
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<contributor.author>Pang, RTK</contributor.author>
<contributor.author>Ng, EHY</contributor.author>
<contributor.author>Lee, KF</contributor.author>
<contributor.author>Koistinen, R</contributor.author>
<contributor.author>Koistinen, H</contributor.author>
<contributor.author>Seppala, M</contributor.author>
<contributor.author>Yeung, WSB</contributor.author>
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<description.abstract>BACKGROUNDGlycodelin-C is a glycodelin isoform isolated from the cumulus matrix. It stimulates spermatozoa-zona pellucida binding. Here, we report the isolation and characterization of a novel glycodelin interacting protein (GIP) from human cumulus matrix.METHODSGIP was purified by liquid chromatograph and identified by mass spectrometry. The interaction of GIP with glycodelin, matrix molecule and spermatozoa were investigated. RESULTS Mass spectrometry analysis suggested that GIP contained the N-terminal region of &#945;2-macroglobulin, confirmed by western blot with anti-&#945;2-macroglobulin antibody. GIP bound to native but not deglycosylated glycodelin-C in native gel electrophoresis, suggesting that the binding was glycosylation-dependent. GIP did not bind to capacitated and uncapacitated human spermatozoa. The cumulus cells could convert exogenous labeled &#945;2-macroglobulin into GIP in vitro. GIP interacted with hyaluronic acid, a major component of the cumulus matrix. Glycodelin-C bound to hyaluronic acid-coated agarose beads in the presence of GIP. Human spermatozoa acquired the hyaluronic acid-GIP-bound glycodelin-C during incubation in vitro. CONCLUSION The hyaluronic acid-GIP complex formed in the cumulus matrix retains and concentrates glycodelin-C in the cumulus matrix for displacing sperm-bound glycodelin-A and-F and stimulating the zona binding activity of the spermatozoa traversing through the cumulus mass.</description.abstract>
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Author Affiliations
  1. Helsingin Yliopisto
  2. The University of Hong Kong